Magnesium in PDB 7m5v: Human ATP13A2 in the Amppnp-Bound Occluded State

The binding sites of Magnesium atom in the Human ATP13A2 in the Amppnp-Bound Occluded State (pdb code 7m5v). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Human ATP13A2 in the Amppnp-Bound Occluded State, PDB code: 7m5v:

Magnesium binding site 1 out of 1 in the Human ATP13A2 in the Amppnp-Bound Occluded State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human ATP13A2 in the Amppnp-Bound Occluded State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1201 b:40.6 occ:1.00 O1G A:ANP1223 2.1 45.2 1.0 HG1 A:THR515 2.2 46.8 1.0 O A:THR515 2.2 46.8 1.0 OD2 A:ASP513 2.3 51.0 1.0 HB3 A:ASP878 2.7 57.6 1.0 OG1 A:THR515 2.9 46.8 1.0 HB2 A:ASP878 2.9 57.6 1.0 CB A:ASP878 3.2 57.6 1.0 C A:THR515 3.3 46.8 1.0 CG A:ASP513 3.5 51.0 1.0 PG A:ANP1223 3.6 45.2 1.0 HD22 A:ASN881 3.7 53.0 1.0 OD2 A:ASP878 3.8 57.6 1.0 CB A:THR515 3.9 46.8 1.0 CG A:ASP878 4.0 57.6 1.0 H A:ASP878 4.0 57.6 1.0 HA3 A:GLY516 4.0 51.4 1.0 H A:THR515 4.0 46.8 1.0 CA A:THR515 4.0 46.8 1.0 HNB1 A:ANP1223 4.1 45.2 1.0 HB2 A:ASP513 4.2 51.0 1.0 O3G A:ANP1223 4.2 45.2 1.0 OD1 A:ASP513 4.2 51.0 1.0 N A:THR515 4.2 46.8 1.0 H A:GLY879 4.3 59.5 1.0 HB A:THR515 4.3 46.8 1.0 N A:GLY516 4.4 51.4 1.0 N3B A:ANP1223 4.4 45.2 1.0 H A:THR517 4.4 53.5 1.0 O2G A:ANP1223 4.5 45.2 1.0 OD1 A:ASN881 4.5 53.0 1.0 CA A:ASP878 4.5 57.6 1.0 CB A:ASP513 4.5 51.0 1.0 ND2 A:ASN881 4.5 53.0 1.0 N A:ASP878 4.6 57.6 1.0 CA A:GLY516 4.7 51.4 1.0 HG23 A:THR517 4.7 53.5 1.0 OD2 A:ASP882 4.8 58.3 1.0 O2B A:ANP1223 4.9 45.2 1.0 N A:GLY879 4.9 59.5 1.0 HA A:THR515 4.9 46.8 1.0 CG A:ASN881 5.0 53.0 1.0

J.Tillinghast, S.Drury, D.Bowser, A.Benn, K.P.K.Lee. Structural Mechanisms For Gating and Ion Selectivity of the Human Polyamine Transporter ATP13A2. Mol.Cell V. 81 4650 2021.
ISSN: ISSN 1097-2765
PubMed: 34715014
DOI: 10.1016/J.MOLCEL.2021.10.002